STRING protein interaction network
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
protein homology
Your Input:
Gene Fusion
AARI_05820Thiamine pyrophosphate binding domain-containing protein; Domain present in thiamine pyrophosphate-requiring enzymes (acetolactate synthase, pyruvate dehydrogenase (cytochrome), glyoxylate carboligase, phosphonopyruvate decarboxylase); Belongs to the TPP enzyme family. (547 aa)    
Predicted Functional Partners:
Ketol-acid reductoisomerase; Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate.
3-isopropylmalate dehydrogenase; Catalyzes the oxidation of 3-carboxy-2-hydroxy-4- methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2- oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate. Belongs to the isocitrate and isopropylmalate dehydrogenases family. LeuB type 2 subfamily.
Acetolactate synthase catalyses the first common step in the biosynthesis of the 3 branched-chain amino acids. The first step involves the condensation of either pyruvate or 2-ketobutyrate with the two-carbon hydroxyethyl fragment derived from another pyruvate molecule, covalently bound to the coenzyme thiamine diphosphate. The resulting products are 2-acetolactate and 2-aceto2-hydroxybutanoate.
Catalyzes the conversion of threonine into 2-oxobutanoate. Involved in isoleucine biosynthesis. The enzyme from a number of sources also acts on L-serine.
2-isopropylmalate synthase; Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3- hydroxy-4-methylpentanoate (2-isopropylmalate); Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 2 subfamily.
Guanidinobutyrase; Catalyses the following reaction: 4-guanidinobutanoate + H(2)O <=> 4-aminobutanoate + urea. The ortholog found in Arthrobacter sp. KUJ 8602 also acts on D-arginine, 3-guanidinopropionate and L-arginine; Belongs to the arginase family.
L-lactate dehydrogenase (cytochrome); Catalyses the conversion of L-lactate to pyruvate. Probable quinone-dependent lactate dehydrogenase, functionning when lactate is used as a carbon and energy source.
Pyruvate dehydrogenase (cytochrome); TPP-binding module. Catalyzes the formation of acetate from pyruvate (catalytic activity: pyruvate + ferricytochrome b1 + H2O = acetate + CO2 + ferrocytochrome b1).
Pyruvate kinase; Catalyses the conversion of phosphoenolpyruvate to pyruvate with the concomitant phosphorylation of ADP to ATP.
Malate dehydrogenase (oxaloacetate-decarboxylating); Catalyzes the oxidative decarboxylation of malate into pyruvate. Uses preferentially NAD and has the ability to decarboxylate oxaloacetate.
Your Current Organism:
Glutamicibacter arilaitensis
NCBI taxonomy Id: 861360
Other names: Arthrobacter arilaitensis CIP 108037, Arthrobacter arilaitensis Re117, G. arilaitensis Re117, Glutamicibacter arilaitensis Re117
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